A. Studies on ATP-Transphosphorylases (Kinases). Comparative physical, chemical and kinetics studies are to be continued or will be undertaken anew on the following series of isolated crystalline enzymes: (1) ATP-creatine transphosphorylase (creatine phosphokinase) isoenzymes (muscle-type, brain-type, and hybrid) from rabbit, calf, normal human tissues, and from dystrophic human tissues; (2) ATP-AMP transphosphorylase (adenylate kinase) from the muscle and liver of rabbit and calf, and from normal and dystrophic man; (3) nucleoside diphosphokinase (nucleoside diphosphate-nucleoside triphosphate transphosphorylase) from yeast; (4) ATP-thiamine pyrophosphokinase from porcine brain and from yeast. In the case of the isoenzymes of ATP-creatin transphosphorylase and of ATP-AMP transphosphorylase, immunological procedures are to be developed to facilitate their analyses in normal and pathological tissues, and their isoenzyme distributions will be explored as a possible aid in the understanding of the genetic basis of the disease(s): the isolated antibodies (anti-enzymes) are to be further explored as suitable tools and probes for the elucidation of the nature of the substrate(s)-binding and catalytic sites of these isoenzymes. Moreover, these enzymes from normal and pathological tissues will likely be of especial interest to those concerned with the genetic problem of Duchenne Muscular Dystrophy in man. B. Studies on NADP-Associated Reactions: (1) Information obtained from studies on the catalyzed reaction of the crystalline NADP-glucose 6-phosphate dehydrogenase from yeast will be complemented by studies on the protein and on its substrates in order to gain some insight into the mechanism of action. A structural analysis of the brewers' yeast enzyme will be initiated and compared with that of the normal human erythrocyte enzyme; and finally, it is hoped that a comparison may be made with the human erythrocyte variant which consequently would be of both genetic and biomedical significance. (2) Studies on the newly isolated crystalline NADPH-Cytochrome c reductase from yeast, in this laboratory are to be continued and compared eventually with its mammalian counterpart from calf liver. It is hoped that these studies may be linked to the final electron acceptor of this microsomal system, (Text Truncated - Exceeds Capacity)